REMARK 2 REMARK 2 RESOLUTION. 2.8 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : MLF REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.8 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.46 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.2 REMARK 3 NUMBER OF REFLECTIONS : 19482 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.2424 REMARK 3 FREE R VALUE : 0.2676 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.9 REMARK 3 FREE R VALUE TEST SET COUNT : 1922 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.8 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.9 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.5 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1668 REMARK 3 BIN R VALUE (WORKING SET) : 0.351 REMARK 3 BIN FREE R VALUE : 0.351 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.4 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 173 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6598 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 106 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 38.9 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.68 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -10.230 REMARK 3 B22 (A**2) : -7.157 REMARK 3 B33 (A**2) : 17.387 REMARK 3 B12 (A**2) : 0.000 REMARK 3 B13 (A**2) : 0.925 REMARK 3 B23 (A**2) : 0.000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.39 REMARK 3 ESD FROM SIGMAA (A) : 0.41 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.60 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.58 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009746 REMARK 3 BOND ANGLES (DEGREES) : 1.75834 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 28.0 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.18 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 2.25 ; 1.50 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.75 ; 2.00 REMARK 3 SIDE-CHAIN BOND (A**2) : 3.35 ; 2.00 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.78 ; 2.50 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.290378 REMARK 3 BSOL : 34.0601 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: DISORDERED REGIONS IN THE PROTEIN REMARK 3 HAVE NOT BEEN MODELED REMARK 4 REMARK 4 2V7H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JUL-07. REMARK 100 THE PDBE ID CODE IS EBI-33305. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-NOV-03 REMARK 200 TEMPERATURE (KELVIN) : 120 REMARK 200 PH : 7.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOMAR REMARK 200 DATA SCALING SOFTWARE : AUTOMAR REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19865 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.80 REMARK 200 RESOLUTION RANGE LOW (A) : 50.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9 REMARK 200 DATA REDUNDANCY : 3.25 REMARK 200 R MERGE (I) : 0.10 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.30 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4 REMARK 200 DATA REDUNDANCY IN SHELL : 3.23 REMARK 200 R MERGE FOR SHELL (I) : 0.38 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.20 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 6FAB REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.5 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRISCL, PH 7.4 WITH 20% REMARK 280 PEG 4000 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.86850 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 4240 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.4 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 4570 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23220 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA B 138 REMARK 465 GLN B 139 REMARK 465 THR B 140 REMARK 465 ASN B 141 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 THR A 8 OG1 CG2 REMARK 470 SER A 10 OG REMARK 470 ASN A 53 CG OD1 ND2 REMARK 470 ASN A 77 CG OD1 ND2 REMARK 470 THR A 93 OG1 CG2 REMARK 470 GLN A 156 CG CD OE1 NE2 REMARK 470 SER B 17 OG REMARK 470 ILE H 20 CG1 CG2 CD1 REMARK 470 HIS H 43 CG ND1 CD2 CE1 NE2 REMARK 470 THR H 97 OG1 CG2 REMARK 470 GLN H 113 CG CD OE1 NE2 REMARK 470 LYS L 107 CG CD CE NZ REMARK 470 LYS L 142 CG CD CE NZ REMARK 470 ASN L 190 CG OD1 ND2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O ASN A 31 - OG1 THR A 51 2.12 REMARK 500 OG SER A 56 - O HOH A 2007 2.15 REMARK 500 NE2 GLN A 80 - OG SER A 171 2.18 REMARK 500 O LEU L 94 - N ARG L 96 2.15 REMARK 500 O ASN H 61 - N LYS H 63 2.16 REMARK 500 O PHE H 154 - N GLU H 156 2.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 REMARK 500 O ARG A 188 OG SER H 57 1656 2.19 REMARK 500 OG SER H 57 O ARG A 188 1646 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 170 N - CA - C ANGL. DEV. = -16.2 DEGREES REMARK 500 GLY B 56 N - CA - C ANGL. DEV. = -17.2 DEGREES REMARK 500 CYS B 96 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 CYS B 148 CA - CB - SG ANGL. DEV. = 7.7 DEGREES REMARK 500 SER L 9 N - CA - C ANGL. DEV. = 19.0 DEGREES REMARK 500 PRO L 95 C - N - CA ANGL. DEV. = -10.1 DEGREES REMARK 500 GLU H 156 N - CA - C ANGL. DEV. = 16.6 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 THR A 7 -83.97 -55.88 REMARK 500 GLN A 27 166.23 179.11 REMARK 500 ASP A 28 143.37 -36.38 REMARK 500 PRO A 40 -162.29 -56.75 REMARK 500 LEU A 47 -47.21 -136.33 REMARK 500 TYR A 49 -158.44 -116.81 REMARK 500 TYR A 50 104.24 11.58 REMARK 500 THR A 51 41.52 35.66 REMARK 500 SER A 52 -160.53 68.64 REMARK 500 ASN A 53 -64.79 66.82 REMARK 500 PRO A 59 155.09 -47.91 REMARK 500 SER A 72 137.51 -178.48 REMARK 500 GLN A 80 39.98 -65.17 REMARK 500 GLU A 81 -7.01 -143.33 REMARK 500 ALA A 84 -168.91 -169.38 REMARK 500 GLN A 89 119.82 -162.40 REMARK 500 ASN A 92 -64.92 -102.93 REMARK 500 THR A 102 93.05 -163.09 REMARK 500 SER A 116 117.47 -162.87 REMARK 500 SER A 153 -154.35 -145.66 REMARK 500 ARG A 155 -129.75 -100.29 REMARK 500 GLN A 156 -28.50 82.92 REMARK 500 SER A 162 111.61 -162.98 REMARK 500 ASP A 170 111.97 -162.02 REMARK 500 SER A 171 75.47 -66.00 REMARK 500 LYS A 183 -38.74 -38.61 REMARK 500 HIS A 198 -166.61 -115.63 REMARK 500 THR A 202 5.09 -65.18 REMARK 500 ALA B 16 -153.90 -114.15 REMARK 500 LYS B 19 79.47 -153.41 REMARK 500 TYR B 27 -178.69 -179.78 REMARK 500 SER B 57 -175.57 33.10 REMARK 500 THR B 58 147.51 142.73 REMARK 500 GLU B 62 38.96 -62.52 REMARK 500 LYS B 63 -52.19 -136.51 REMARK 500 ALA B 72 -109.26 -45.20 REMARK 500 ASP B 73 85.97 70.12 REMARK 500 SER B 75 -72.78 -57.01 REMARK 500 ASN B 77 74.10 76.10 REMARK 500 ALA B 92 -170.86 -175.55 REMARK 500 TRP B 102 111.82 87.71 REMARK 500 ALA B 105 146.44 75.15 REMARK 500 SER B 120 147.01 -177.53 REMARK 500 SER B 121 41.99 -101.36 REMARK 500 PRO B 157 -159.41 -122.03 REMARK 500 SER B 180 89.00 -166.99 REMARK 500 ASP B 181 -18.69 65.19 REMARK 500 HIS B 207 85.97 -155.45 REMARK 500 PRO B 220 152.02 -37.30 REMARK 500 GLN L 6 36.92 -99.91 REMARK 500 THR L 7 -86.54 73.67 REMARK 500 THR L 8 14.68 173.89 REMARK 500 GLN L 27 143.28 174.08 REMARK 500 ASP L 28 124.74 -30.46 REMARK 500 ASN L 31 -5.29 72.20 REMARK 500 TYR L 50 86.75 52.81 REMARK 500 SER L 52 -169.13 69.28 REMARK 500 ASN L 53 -46.23 85.21 REMARK 500 SER L 72 117.88 -167.82 REMARK 500 THR L 74 108.69 -162.14 REMARK 500 GLU L 81 2.01 -62.57 REMARK 500 ALA L 84 -163.18 -170.05 REMARK 500 PRO L 95 103.16 -56.67 REMARK 500 THR L 126 46.44 -95.43 REMARK 500 ASN L 138 73.38 37.82 REMARK 500 TYR L 140 139.35 178.41 REMARK 500 PRO L 141 175.90 -51.20 REMARK 500 SER L 153 -105.65 -145.43 REMARK 500 ARG L 155 -101.44 -141.31 REMARK 500 GLN L 156 -91.87 61.10 REMARK 500 SER L 162 140.34 -179.32 REMARK 500 GLN L 166 121.75 -36.64 REMARK 500 LYS L 169 -88.19 -70.36 REMARK 500 ASP L 170 -149.84 -80.55 REMARK 500 LYS L 199 56.30 -90.79 REMARK 500 PRO L 204 136.60 -39.69 REMARK 500 ASN L 212 75.06 -110.12 REMARK 500 GLU L 213 43.70 -160.64 REMARK 500 ALA H 16 -156.28 -70.77 REMARK 500 PHE H 29 -58.38 -17.63 REMARK 500 GLU H 62 17.97 -54.65 REMARK 500 THR H 69 105.18 -175.64 REMARK 500 ALA H 72 -156.60 -121.31 REMARK 500 ASP H 73 102.96 179.63 REMARK 500 THR H 74 -8.88 -53.82 REMARK 500 SER H 85 74.01 32.55 REMARK 500 GLU H 89 -4.83 -59.98 REMARK 500 ALA H 92 178.97 176.63 REMARK 500 TRP H 102 -60.54 75.84 REMARK 500 TYR H 106 55.79 -55.67 REMARK 500 THR H 124 139.74 -36.64 REMARK 500 SER H 136 -69.09 -19.46 REMARK 500 ALA H 138 39.77 -65.01 REMARK 500 GLN H 139 130.27 -23.78 REMARK 500 THR H 140 88.65 55.63 REMARK 500 MET H 143 143.72 166.63 REMARK 500 CYS H 148 99.68 174.98 REMARK 500 PHE H 154 -124.00 -127.20 REMARK 500 PRO H 155 49.55 5.34 REMARK 500 GLU H 156 -66.54 13.70 REMARK 500 SER H 166 -75.57 -7.66 REMARK 500 SER H 168 -43.94 -153.29 REMARK 500 GLN H 179 -76.21 -87.88 REMARK 500 ASP H 181 -2.18 85.74 REMARK 500 PRO H 195 -80.21 -46.45 REMARK 500 HIS H 207 89.84 -165.86 REMARK 500 LYS H 213 106.32 -168.93 REMARK 500 PRO H 220 -178.45 -39.93 REMARK 500 ARG H 221 -151.78 77.57 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 SER L 9 23.9 L L OUTSIDE RANGE REMARK 500 LEU L 94 24.1 L L OUTSIDE RANGE REMARK 500 GLU H 156 23.3 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 700 REMARK 700 SHEET REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, REMARK 700 TWO SHEETS ARE DEFINED.